title: Purification and characterization of cathepsin L-like enzyme from the muscle of anchovy, Engraulis japonica.
abstract: Results relative to inhibitory effects and substrate specificity indicated that a protease from the muscle of anchovy, Engraulis japonica, was a cathepsin L-like enzyme. The enzyme was activated by thiol reagents and inhibited by thiol-blocking reagents. The molecular weight was estimated to be 25.8 kDa by SDS-PAGE. The enzyme exhibited its maximal activity at pH 6.0 and 50 degrees C for casein and N-benzoyl-D, L-arginine-beta-naphthylamide. The enzyme hydrolyzed at the position of Phe1, Asn3, Val13, Glu14, Val19 and Gly24 of the insulin beta-chain. The K'm and kcat of the enzyme were 73.4 microM and 0.5 microM/min, respectively, toward Z-Phe-Arg-MNap.
authors.affiliation: Department of Food Science, Gyeongsang National University, Kyeongnam, Korea.
authors.forename: M S
authors.initials: MS
authors.lastname: Heu
authors.forename: H R
authors.initials: HR
authors.lastname: Kim
authors.forename: D M
authors.initials: DM
authors.lastname: Cho
authors.forename: J S
authors.initials: JS
authors.lastname: Godber
authors.forename: J H
authors.initials: JH
authors.lastname: Pyeun
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D056668:Cathepsin L; D002403:Cathepsins / Q000378:metabolism*; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D010450:Endopeptidases; D005399:Fishes; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009132:Muscles / Q000737:chemistry / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature
chemical_list: D000596:Amino Acids; D015853:Cysteine Proteinase Inhibitors; D002403:Cathepsins; D010450:Endopeptidases; D003546:Cysteine Endopeptidases; D056668:Cathepsin L